Saccharification Kinetics at Optimised Conditions of Tapioca by Glucoamylase Immobilised on Mesostructured Cellular Foam Silica

As insoluble substrates such as tapioca can be used to make chemical compounds, saccharification of tapioca by glucoamylase immobilised on mesostructured cellular foam (MCF) silica using Box-Behnken Design of experiment was conducted to optimize this process so that the experimental results can be u...

Full description

Bibliographic Details
Main Authors: J. Agustian, L. Hermide
Format: Article
Language:English
Published: al-Farabi Kazakh National University 2018-12-01
Series:Eurasian Chemico-Technological Journal 
Online Access:http://ect-journal.kz/index.php/ectj/article/view/764
id doaj-fa26bb41fa8d456e83d704e9adb839cb
record_format Article
spelling doaj-fa26bb41fa8d456e83d704e9adb839cb2020-11-24T23:32:57Zengal-Farabi Kazakh National UniversityEurasian Chemico-Technological Journal 1562-39202522-48672018-12-0120431131810.18321/ectj764764Saccharification Kinetics at Optimised Conditions of Tapioca by Glucoamylase Immobilised on Mesostructured Cellular Foam SilicaJ. Agustian0L. Hermide1Department of Chemical Engineering, Universitas LampungDepartment of Chemical Engineering, Universitas LampungAs insoluble substrates such as tapioca can be used to make chemical compounds, saccharification of tapioca by glucoamylase immobilised on mesostructured cellular foam (MCF) silica using Box-Behnken Design of experiment was conducted to optimize this process so that the experimental results can be used to develop large-scale operations. The experiments gave dextrose equivalent (DE) values of 6.15–69.50% (w/w). Factors of pH and temperature affected the process highly. The suggested quadratic polynomial model is significant and considered acceptable (R2 = 99.78%). Justification of the model confirms its validity and adequacy where the predicted DE shows a good agreement with the experimental results. The kinetic constants (Vmax, KM) produced by the immobilised enzyme differed highly from the values yielded by free glucoamylase indicating reduction of substrate access to enzyme active sites had occurred.http://ect-journal.kz/index.php/ectj/article/view/764
collection DOAJ
language English
format Article
sources DOAJ
author J. Agustian
L. Hermide
spellingShingle J. Agustian
L. Hermide
Saccharification Kinetics at Optimised Conditions of Tapioca by Glucoamylase Immobilised on Mesostructured Cellular Foam Silica
Eurasian Chemico-Technological Journal 
author_facet J. Agustian
L. Hermide
author_sort J. Agustian
title Saccharification Kinetics at Optimised Conditions of Tapioca by Glucoamylase Immobilised on Mesostructured Cellular Foam Silica
title_short Saccharification Kinetics at Optimised Conditions of Tapioca by Glucoamylase Immobilised on Mesostructured Cellular Foam Silica
title_full Saccharification Kinetics at Optimised Conditions of Tapioca by Glucoamylase Immobilised on Mesostructured Cellular Foam Silica
title_fullStr Saccharification Kinetics at Optimised Conditions of Tapioca by Glucoamylase Immobilised on Mesostructured Cellular Foam Silica
title_full_unstemmed Saccharification Kinetics at Optimised Conditions of Tapioca by Glucoamylase Immobilised on Mesostructured Cellular Foam Silica
title_sort saccharification kinetics at optimised conditions of tapioca by glucoamylase immobilised on mesostructured cellular foam silica
publisher al-Farabi Kazakh National University
series Eurasian Chemico-Technological Journal 
issn 1562-3920
2522-4867
publishDate 2018-12-01
description As insoluble substrates such as tapioca can be used to make chemical compounds, saccharification of tapioca by glucoamylase immobilised on mesostructured cellular foam (MCF) silica using Box-Behnken Design of experiment was conducted to optimize this process so that the experimental results can be used to develop large-scale operations. The experiments gave dextrose equivalent (DE) values of 6.15–69.50% (w/w). Factors of pH and temperature affected the process highly. The suggested quadratic polynomial model is significant and considered acceptable (R2 = 99.78%). Justification of the model confirms its validity and adequacy where the predicted DE shows a good agreement with the experimental results. The kinetic constants (Vmax, KM) produced by the immobilised enzyme differed highly from the values yielded by free glucoamylase indicating reduction of substrate access to enzyme active sites had occurred.
url http://ect-journal.kz/index.php/ectj/article/view/764
work_keys_str_mv AT jagustian saccharificationkineticsatoptimisedconditionsoftapiocabyglucoamylaseimmobilisedonmesostructuredcellularfoamsilica
AT lhermide saccharificationkineticsatoptimisedconditionsoftapiocabyglucoamylaseimmobilisedonmesostructuredcellularfoamsilica
_version_ 1725532622685208576